PGK2_MOUSE
ID PGK2_MOUSE Reviewed; 417 AA.
AC P09041; Q5RKV3; Q6P8V2;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Phosphoglycerate kinase 2;
DE EC=2.7.2.3 {ECO:0000269|PubMed:2823118};
DE AltName: Full=Phosphoglycerate kinase, testis specific;
GN Name=Pgk2; Synonyms=Pgk-2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=2823118; DOI=10.1128/mcb.7.9.3107-3112.1987;
RA Boer P.H., Adra C.N., Lau Y.-F.C., McBurney M.W.;
RT "The testis-specific phosphoglycerate kinase gene pgk-2 is a recruited
RT retroposon.";
RL Mol. Cell. Biol. 7:3107-3112(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX PubMed=2166582; DOI=10.1016/0167-4781(90)90106-c;
RA Tamaru M., Nagao Y., Taira M., Tatibana M., Masamune Y., Nakanishi Y.;
RT "Selective activation of testis-specific genes in cultured rat
RT spermatogenic cells.";
RL Biochim. Biophys. Acta 1049:331-338(1990).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=3453121; DOI=10.1038/326501a0;
RA McCarrey J.R., Thomas K.;
RT "Human testis-specific PGK gene lacks introns and possesses characteristics
RT of a processed gene.";
RL Nature 326:501-504(1987).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19759366; DOI=10.1095/biolreprod.109.079699;
RA Danshina P.V., Geyer C.B., Dai Q., Goulding E.H., Willis W.D., Kitto G.B.,
RA McCarrey J.R., Eddy E.M., O'Brien D.A.;
RT "Phosphoglycerate kinase 2 (PGK2) is essential for sperm function and male
RT fertility in mice.";
RL Biol. Reprod. 82:136-145(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-417 ALONE AND IN COMPLEX WITH
RP PHOSPHOGLYCERATE AND ATP, SUBUNIT, AND SUBSTRATE-BINDING SITES.
RX PubMed=18004764; DOI=10.1002/prot.21801;
RA Sawyer G.M., Monzingo A.F., Poteet E.C., O'Brien D.A., Robertus J.D.;
RT "X-ray analysis of phosphoglycerate kinase 2, a sperm-specific isoform from
RT Mus musculus.";
RL Proteins 71:1134-1144(2008).
CC -!- FUNCTION: Essential for sperm motility and male fertility but is not
CC required for the completion of spermatogenesis (PubMed:19759366).
CC {ECO:0000269|PubMed:19759366}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC Evidence={ECO:0000305|PubMed:2823118};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18004764}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Testis and sperm. Localized on the principle piece
CC in the sperm (at protein level). Testis-specific.
CC {ECO:0000269|PubMed:19759366, ECO:0000269|PubMed:3453121}.
CC -!- DISRUPTION PHENOTYPE: Mice display greatly reduced ATP levels in sperm,
CC severely impaired sperm motility and are infertile. No alteration in
CC testis histology, sperm counts, or sperm ultrastructure seen.
CC {ECO:0000269|PubMed:19759366}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000305}.
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DR EMBL; M17299; AAA39920.1; -; Genomic_DNA.
DR EMBL; M18654; AAA39921.1; -; mRNA.
DR EMBL; AK133436; BAE21656.1; -; mRNA.
DR EMBL; CH466559; EDL23381.1; -; Genomic_DNA.
DR EMBL; BC052343; AAH52343.1; -; mRNA.
DR EMBL; BC061054; AAH61054.1; -; mRNA.
DR EMBL; X55310; CAA39014.1; -; Genomic_DNA.
DR CCDS; CCDS28782.1; -.
DR PIR; A27775; A27775.
DR RefSeq; NP_112467.2; NM_031190.2.
DR PDB; 2P9Q; X-ray; 2.70 A; A/B=2-417.
DR PDB; 2P9T; X-ray; 2.00 A; A=2-417.
DR PDB; 2PAA; X-ray; 2.70 A; A/B=2-417.
DR PDBsum; 2P9Q; -.
DR PDBsum; 2P9T; -.
DR PDBsum; 2PAA; -.
DR AlphaFoldDB; P09041; -.
DR SMR; P09041; -.
DR BioGRID; 202135; 14.
DR IntAct; P09041; 1.
DR STRING; 10090.ENSMUSP00000033585; -.
DR iPTMnet; P09041; -.
DR PhosphoSitePlus; P09041; -.
DR SwissPalm; P09041; -.
DR REPRODUCTION-2DPAGE; IPI00555060; -.
DR REPRODUCTION-2DPAGE; P09041; -.
DR EPD; P09041; -.
DR jPOST; P09041; -.
DR MaxQB; P09041; -.
DR PaxDb; P09041; -.
DR PeptideAtlas; P09041; -.
DR PRIDE; P09041; -.
DR ProteomicsDB; 288106; -.
DR Antibodypedia; 30847; 250 antibodies from 28 providers.
DR DNASU; 18663; -.
DR Ensembl; ENSMUST00000033585; ENSMUSP00000033585; ENSMUSG00000031233.
DR GeneID; 18663; -.
DR KEGG; mmu:18663; -.
DR UCSC; uc008cof.2; mouse.
DR CTD; 5232; -.
DR MGI; MGI:97563; Pgk2.
DR VEuPathDB; HostDB:ENSMUSG00000031233; -.
DR eggNOG; KOG1367; Eukaryota.
DR GeneTree; ENSGT00390000008820; -.
DR HOGENOM; CLU_025427_0_0_1; -.
DR InParanoid; P09041; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 838642at2759; -.
DR PhylomeDB; P09041; -.
DR TreeFam; TF300489; -.
DR BRENDA; 2.7.2.3; 3474.
DR Reactome; R-MMU-70171; Glycolysis.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR SABIO-RK; P09041; -.
DR UniPathway; UPA00109; UER00185.
DR BioGRID-ORCS; 18663; 2 hits in 71 CRISPR screens.
DR EvolutionaryTrace; P09041; -.
DR PRO; PR:P09041; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P09041; protein.
DR Bgee; ENSMUSG00000031233; Expressed in spermatid and 9 other tissues.
DR Genevisible; P09041; MM.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0035686; C:sperm fibrous sheath; IDA:MGI.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IDA:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IMP:MGI.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR DisProt; DP02749; -.
DR Gene3D; 3.40.50.1260; -; 3.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; Glycolysis; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..417
FT /note="Phosphoglycerate kinase 2"
FT /id="PRO_0000145836"
FT BINDING 24..26
FT /ligand="substrate"
FT BINDING 39
FT /ligand="substrate"
FT BINDING 63..66
FT /ligand="substrate"
FT BINDING 123
FT /ligand="substrate"
FT BINDING 171
FT /ligand="substrate"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18004764"
FT BINDING 313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18004764"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18004764"
FT BINDING 373..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18004764"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 86
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 196
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 267
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT CONFLICT 151
FT /note="Q -> R (in Ref. 1; AAA39920)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="T -> M (in Ref. 1; AAA39920/AAA39921)"
FT /evidence="ECO:0000305"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2P9Q"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2P9Q"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2P9T"
FT TURN 126..130
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 188..202
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:2P9T"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:2P9Q"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 284..293
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:2P9T"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 318..329
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 350..364
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 375..382
FT /evidence="ECO:0007829|PDB:2P9T"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:2P9T"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 396..402
FT /evidence="ECO:0007829|PDB:2P9T"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:2P9T"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:2P9T"
SQ SEQUENCE 417 AA; 44853 MW; BC3FACE559798B53 CRC64;
MALSAKLTLD KVDLKGKRVI MRVDFNVPMK NNQITNNQRI KAAIPSIKHC LDNGAKSVVL
MSHLGRPDGI PMPDKYSLEP VADELKSLLN KDVIFLKDCV GPEVEQACAN PDNGSIILLE
NLRFHVEEEG KGKDSSGKKI SADPAKVEAF QASLSKLGDV YVNDAFGTAH RAHSSTVGVN
LPQKASGFLM KKELDYFSKA LEKPERPFLA ILGGAKVKDK IQLIKNMLDK VNFMIIGGGM
AYTFLKELKN MQIGASLFDE EGATIVKEIM EKAEKNGVKI VFPVDFVTGD KFDENAKVGQ
ATIESGIPSG WMGLDCGPES IKINAQIVAQ AKLIVWNGPI GVFEWDAFAK GTKALMDEVV
KATSNGCVTI IGGGDTATCC AKWGTEDKVS HVSTGGGASL ELLEGKILPG VEALSNM
